A spindle pole body-associated protein, SNAD, affects septation and conidiation in Aspergillus nidulans |
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Authors: | Liu B Morris N R |
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Institution: | (1) Department of Pharmacology, UMDNJ/RWJMS, Piscataway, NJ 08854, USA, US;(2) Section of Plant Biology, University of California at Davis, Davis, CA 95616, USA E-mail: bliu@ucdavis.edu, US |
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Abstract: | The nudA1 mutation in the cytoplasmic dynein heavy chain gene inhibits nuclear migration, colony growth and asexual sporulation (conidiation)
in the filamentous fungus Aspergillus nidulans. It also alters the location of the first cell division event (septation) and prevents nucleation of tip cells. We showed
previously that a suppressor of nudA1, snaD290, partially reversed the nuclear migration defect and partially restored colony growth. We have now demonstrated that the
snaD290 mutation also delays septation and restores the septum to its normal position, allowing tip cells to be nucleated. Although
snaD290 does not affect nuclear migration or vegetative hyphal growth, it almost completely inhibits conidiation. We propose that
the SNAD protein participates in septation, and is essential for asexual spore formation. SnaD encodes a novel 76-kDa coiled-coil protein (SNAD) that is located at the spindle pole body throughout the cell cycle. Therefore,
our results suggest that proteins at the spindle pole body are likely to be involved in temporal regulation of septation in
A. nidulans.
Received: 5 October 1999 / Accepted: 28 December 1999 |
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Keywords: | Cytokinesis Cytoplasmic dynein Septation Spindle pole body Aspergillus |
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